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Related Experiment Videos

Alternative splicing generates at least five different isoforms of the human basic-FGF receptor.

A Eisemann1, J A Ahn, G Graziani

  • 1Laboratory of Cellular and Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.

Oncogene
|July 1, 1991
PubMed
Summary

Alternative splicing generates diverse fibroblast growth factor (FGF) receptor isoforms in human cells. These variants, including transmembrane and secreted forms, arise from a single genetic locus and exhibit varied expression patterns.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Fibroblast growth factors (FGFs) are crucial polypeptide mitogens influencing cell proliferation, angiogenesis, differentiation, and neuronal survival.
  • Keratinocyte growth factor (KGF) is a specific FGF mitogen for epithelial cells, distinct from fibroblast interactions.
  • Understanding FGF receptor diversity is key to comprehending FGF signaling pathways.

Purpose of the Study:

  • To investigate the interactions between KGF and its receptor.
  • To isolate and characterize FGF receptors from human keratinocytes and fibroblasts.
  • To identify and analyze the different variants of FGF receptors generated in human cells.

Main Methods:

  • Isolation of KGF and FGF receptors from human keratinocytes and fibroblasts.

Related Experiment Videos

  • Analysis of FGF receptor variants using molecular techniques.
  • Characterization of receptor structure, including Ig-like domains and transmembrane regions.
  • Assessment of transcript expression levels in various cell types.

    • Main Results:

    • Five distinct FGF receptor variants were isolated from human fibroblasts, all originating from a single genetic locus.
    • Four variants encode transmembrane receptors, differing in the number of Ig-like domains (two or three) and a two-codon insertion within the ligand-binding domain.
    • The fifth variant encodes a secreted, truncated receptor lacking the transmembrane domain.
    • Differential expression levels of long and short receptor isoforms were observed across various cell types.

    Conclusions:

    • Alternative splicing is a primary mechanism generating diverse FGF receptor isoforms in human cells.
    • FGF receptor heterogeneity, including transmembrane and secreted forms, contributes to the complexity of FGF signaling.
    • The identified receptor variants possess distinct structural features that likely influence their signaling capabilities and ligand interactions.